Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes
Howard Hughes Medical Institute · University of Illinois Urbana-Champaign
Abstract
Lanthipeptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) that display a wide variety of biological activities, from antimicrobial to antiallodynic. Lanthipeptides that display antimicrobial activity are called lantibiotics. The post-translational modification reactions of lanthipeptides include dehydration of Ser and Thr residues to dehydroalanine and dehydrobutyrine, a transformation that is carried out in three unique ways in different classes of lanthipeptides. In a cyclization process, Cys residues then attack the dehydrated residues to generate the lanthionine and methyllanthionine thioether cross-linked amino acids from which lanthipeptides derive their name. The…
Citation impact
- FWCI
- 16.82
- Percentile
- 100%
- References
- 495
Authors
4- LMLindsay M. RepkaCorresponding
Howard Hughes Medical Institute, University of Illinois Urbana-Champaign
- JRJonathan R. Chekan
Howard Hughes Medical Institute, University of Illinois Urbana-Champaign
- SKSatish K. Nair
Howard Hughes Medical Institute, University of Illinois Urbana-Champaign
- WAWilfred A. van der Donk
Howard Hughes Medical Institute, University of Illinois Urbana-Champaign
Topics & keywords
- Lantibiotics
- Dehydroalanine
- Chemistry
- Lanthionine
- Thioether
- Enzyme
- Semisynthesis
- Combinatorial chemistry